Amino Acids, Proteins, and Enzymes Lecture

Vocabulary flashcards covering the structure and function of amino acids and proteins, types of biochemical reactions, and enzyme kinetics and inhibition.

Amino Acids

The building blocks of proteins consisting of central carbons joined to carboxyl and amino groups with a variable R group.

Essential Amino Acids

Amino acids that can not be synthesised by the body.

Non-essential Amino Acids

Amino acids that can be synthesised by the body.

Proteins

Polymers of amino acids linked by peptide bonds.

Primary Structure

The sequence of amino acids in a protein, held together only by peptide bonds.

Secondary Structure

Local folding of a protein into alpha-helices and beta-sheets, maintained by hydrogen bonding.

Tertiary Structure

The overall 3D shape of a single polypeptide involving multiple interactions.

Quaternary Structure

The arrangement of multiple polypeptides involving multiple interactions except disulfide bridge.

Enzymatic Function

A functional role of proteins to catalyze biochemical reactions, such as amylase.

Structural Function

A functional role of proteins to provide support and shape, such as collagen.

Transport Function

A functional role of proteins to carry molecules, such as haemoglobin.

Signalling Function

A functional role of proteins to act as hormones and receptors, such as insulin.

Biochemical Reactions

Processes involving the transformation of substrates into products, essential for metabolism.

CATABOLIC

Metabolic pathways involved in the breakdown of substances.

ANABOLIC

Metabolic pathways involved in the synthesis of substances.

Enzymes

Biological catalysts that speed up biochemical reactions without changing themselves by lowering the activation energy.

Activation Energy

The energy required for a reaction to occur, which enzymes lower by providing an alternative pathway.

Active Sites

Specific regions on an enzyme where substrates bind during a reaction.

Lock and Key Fit

A model used to describe the specificity of an enzyme's active site to its substrate.

Induced Fit

A model used to describe the specificity and binding mechanism between an enzyme and its substrate.

Competitive Inhibitors

Molecules that shortly bind to active sights of an enzyme to prevent substrate binding.

Non-competitive Inhibitors

Molecules that bind to the allosteric site of an enzyme, changing the enzyme's shape so the substrate can no longer bind.

Allosteric Site

The specific site on an enzyme where a non-competitive inhibitor binds.